Wobble uridine modifications–a reason to live, a reason to die?!
Open Access
- 13 April 2017
- journal article
- review article
- Published by Taylor & Francis Ltd in RNA Biology
- Vol. 14 (9), 1209-1222
- https://doi.org/10.1080/15476286.2017.1295204
Abstract
Wobble uridines (U34) are generally modified in all species. U34 modifications can be essential in metazoans but are not required for viability in fungi. In this review, we provide an overview on the types of modifications and how they affect the physico-chemical properties of wobble uridines. We describe the molecular machinery required to introduce these modifications into tRNA posttranscriptionally and discuss how posttranslational regulation may affect the activity of the modifying enzymes. We highlight the activity of anticodon specific RNases that target U34 containing tRNA. Finally, we discuss how defects in wobble uridine modifications lead to phenotypes in different species. Importantly, this review will mainly focus on the cytoplasmic tRNAs of eukaryotes. A recent review has extensively covered their bacterial and mitochondrial counterparts. 1Keywords
This publication has 138 references indexed in Scilit:
- Translational Control of Cell Division by ElongatorCell Reports, 2012
- Human tRNALys3UUU Is Pre-Structured by Natural Modifications for Cognate and Wobble Codon Binding through Keto–Enol TautomerismJournal of Molecular Biology, 2012
- Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteinsNature Communications, 2012
- Mechanistic understanding of Pyrococcus horikoshiiDph2, a [4Fe–4S] enzyme required for diphthamidebiosynthesisMolecular BioSystems, 2010
- PhosphoPep—a database of protein phosphorylation sites in model organismsNature Biotechnology, 2008
- Urm1 at the crossroad of modificationsEMBO Reports, 2008
- RNA Repair: An Antidote to Cytotoxic Eukaryal RNA DamageMolecular Cell, 2008
- Biochemical and Structural Characterization of a Novel Family of Cystathionine β-Synthase Domain Proteins Fused to a Zn Ribbon-Like DomainJournal of Molecular Biology, 2008
- Trm9-Catalyzed tRNA Modifications Link Translation to the DNA Damage ResponseMolecular Cell, 2007
- Solution structure of Urm1 and its implications for the origin of protein modifiersProceedings of the National Academy of Sciences of the United States of America, 2006